title: Polypeptide N-acetylgalactosaminyl transferase 3 independently predicts high-grade tumours and poor prognosis in patients with renal cell carcinomas.
abstract: BACKGROUND
  The polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts) family of enzymes regulates the initial steps of mucin-type O-glycosylation. N-acetylgalactosaminyltransferases might show novel patterns of GalNAc-T glycosylation on tumour-derived proteins, which could influence cancer biology, but its mechanisms are unclear. We investigated the association of GalNAc-T3 and -T6 expressions with clinicopathological features and prognoses of patients with renal cell carcinomas (RCCs).
  
  
  METHODS
  Expressions of GalNAc-T3/6 and cell-adhesion molecules were analysed immunohistochemically in 254 paraffin-embedded tumour samples of patients with RCC.
  
  
  RESULTS
  Of 138 GalNAc-T3+ cases, 46 revealed significant co-expression with GalNAc-T6. N-acetylgalactosaminyltransferases-3+ expression showed a close relationship to poor clinical performance and large tumour size, or pathologically high Fuhrman's grading, and presence of vascular invasion and necrosis. The GalNAc-T3-positivity potentially suppressed adhesive effects with a significantly low β-catenin expression. Univariate and multivariate analyses showed the GalNAc-T3+ group, but not the GalNAc-T6+ group, to have significantly worse survival rates.
  
  
  CONCLUSIONS
  N-acetylgalactosaminyltransferases-3 expression independently predicts high-grade tumour and poor prognosis in patients with RCC, and may offer a therapeutic target against RCC.
authors.affiliation: Department of Pathology and Cell Biology, School of Medicine, University of Occupational and Environmental Health, Kitakyushu, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Kitada
authors.forename: S
authors.initials: S
authors.lastname: Yamada
authors.forename: A
authors.initials: A
authors.lastname: Kuma
authors.forename: S
authors.initials: S
authors.lastname: Ouchi
authors.forename: T
authors.initials: T
authors.lastname: Tasaki
authors.forename: A
authors.initials: A
authors.lastname: Nabeshima
authors.forename: H
authors.initials: H
authors.lastname: Noguchi
authors.forename: K-Y
authors.initials: KY
authors.lastname: Wang
authors.forename: S
authors.initials: S
authors.lastname: Shimajiri
authors.forename: R
authors.initials: R
authors.lastname: Nakano
authors.forename: H
authors.initials: H
authors.lastname: Izumi
authors.forename: K
authors.initials: K
authors.lastname: Kohno
authors.forename: T
authors.initials: T
authors.lastname: Matsumoto
authors.forename: Y
authors.initials: Y
authors.lastname: Sasaguri
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D014408:Biomarkers, Tumor / Q000235:genetics / Q000378:metabolism*; D002292:Carcinoma, Renal Cell / Q000201:enzymology / Q000473:pathology*; D045744:Cell Line, Tumor; D015331:Cohort Studies; D005260:Female; D006801:Humans; D007680:Kidney Neoplasms / Q000201:enzymology / Q000473:pathology*; D008297:Male; D008875:Middle Aged; D017350:N-Acetylgalactosaminyltransferases / Q000235:genetics / Q000378:metabolism*; D060787:Neoplasm Grading; D011379:Prognosis; D012189:Retrospective Studies; D000097763:Polypeptide N-acetylgalactosaminyltransferase
chemical_list: D014408:Biomarkers, Tumor; D017350:N-Acetylgalactosaminyltransferases; D000097763:Polypeptide N-acetylgalactosaminyltransferase